메뉴 건너뛰기




Volumn 2, Issue 3, 2001, Pages 188-194

Regulation of cellular polyamines by antizyme

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE PROTEINASE; ENZYME INHIBITOR; MULTIENZYME COMPLEX; ORNITHINE DECARBOXYLASE; POLYAMINE; PROTEASOME;

EID: 0035291218     PISSN: 14710072     EISSN: None     Source Type: Journal    
DOI: 10.1038/35056508     Document Type: Review
Times cited : (315)

References (45)
  • 1
    • 0345955882 scopus 로고
    • Induction of a protein inhibitor to ornithine decarboxytase by the end products of its reaction
    • Heller, J. S., Fong, W. F. & Canellakis, E. S. Induction of a protein inhibitor to ornithine decarboxytase by the end products of its reaction. Proc. Natl Acad. Sci. USA 73, 1858-1862 (1976).
    • (1976) Proc. Natl Acad. Sci. USA , vol.73 , pp. 1858-1862
    • Heller, J.S.1    Fong, W.F.2    Canellakis, E.S.3
  • 4
    • 0019778476 scopus 로고
    • Cadaverine and putrescine initiate the burial of dead conspecifics by rats
    • Pinel, J. P. J., Gorzalka, B. B. & Ladak, F. Cadaverine and putrescine initiate the burial of dead conspecifics by rats. Physiol. Behav. 27, 819-824 (1981).
    • (1981) Physiol. Behav. , vol.27 , pp. 819-824
    • Pinel, J.P.J.1    Gorzalka, B.B.2    Ladak, F.3
  • 5
    • 0021103647 scopus 로고
    • The preparation and properties of gel-filtered rabbit-reticulocyte lysate protein-synthesis systems
    • Jackson, R. J., Campbell, E. A., Herbert, P. & Hunt, T. The preparation and properties of gel-filtered rabbit-reticulocyte lysate protein-synthesis systems. Eur. J. Biochem. 131, 289-301 (1983).
    • (1983) Eur. J. Biochem. , vol.131 , pp. 289-301
    • Jackson, R.J.1    Campbell, E.A.2    Herbert, P.3    Hunt, T.4
  • 6
    • 0025786779 scopus 로고
    • Estimation of polyamine binding to macromolecules and ATP in bovine lymphocytes and rat liver
    • Watanabe, S., Kusama-Eguchi, K., Kobayashi, H. & Igarashi, K. Estimation of polyamine binding to macromolecules and ATP in bovine lymphocytes and rat liver. J. Biol. Chem. 266, 20803-20809 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 20803-20809
    • Watanabe, S.1    Kusama-Eguchi, K.2    Kobayashi, H.3    Igarashi, K.4
  • 7
    • 0027370986 scopus 로고
    • Is hypusine essential for eukaryotic cell proliferation?
    • Park, M. H., Wolff, E. C. & Folk, J. E. Is hypusine essential for eukaryotic cell proliferation? Trends Biochem. Sci. 18, 475-479 (1993).
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 475-479
    • Park, M.H.1    Wolff, E.C.2    Folk, J.E.3
  • 8
    • 0034663939 scopus 로고    scopus 로고
    • Exportin 4: A mediator of a novel nuclear export pathway in higher eukaryotes
    • Lipowsky, G. et al. Exportin 4: a mediator of a novel nuclear export pathway in higher eukaryotes. EMBO J. 19, 4362-4371 (2000).
    • (2000) EMBO J. , vol.19 , pp. 4362-4371
    • Lipowsky, G.1
  • 9
    • 0027984375 scopus 로고
    • Potassium channel block by cytoplasmic polyamines as the mechanism of intrinsic rectification
    • Lopatin, A. N., Makhina, E. N. & Nichols, C. G. Potassium channel block by cytoplasmic polyamines as the mechanism of intrinsic rectification. Nature 372, 366-369 (1994).
    • (1994) Nature , vol.372 , pp. 366-369
    • Lopatin, A.N.1    Makhina, E.N.2    Nichols, C.G.3
  • 10
    • 0033569769 scopus 로고    scopus 로고
    • Functional interaction between GCN5 and polyamines: A new role for core histone acetylation
    • Pollard, K. J., Samuels, M. L., Crowley, K. A., Hansen, J. C. & Peterson, C. L. Functional interaction between GCN5 and polyamines: a new role for core histone acetylation. EMBO J. 18, 5622-5633 (1999).
    • (1999) EMBO J. , vol.18 , pp. 5622-5633
    • Pollard, K.J.1    Samuels, M.L.2    Crowley, K.A.3    Hansen, J.C.4    Peterson, C.L.5
  • 11
    • 0027462162 scopus 로고
    • Enhancement of the spermidine uptake system and lethal effects of spermidine overaccumulation in ornithine decarboxylase-overproducing L1210 cells under hyposmotic stress
    • Poulin, R. L., Coward, J. K., Lakanen, J. R. & Pegg, A. E. Enhancement of the spermidine uptake system and lethal effects of spermidine overaccumulation in ornithine decarboxylase-overproducing L1210 cells under hyposmotic stress. J. Biol. Chem. 268, 4690-4698 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 4690-4698
    • Poulin, R.L.1    Coward, J.K.2    Lakanen, J.R.3    Pegg, A.E.4
  • 12
  • 13
    • 0030052923 scopus 로고    scopus 로고
    • Ornithine decarboxylase antizyme: A novel type of regulatory protein
    • Hayashi, S., Murakami, Y. & Matsufuji, S. Ornithine decarboxylase antizyme: a novel type of regulatory protein. Trends Biochem. Sci. 21, 27-30 (1996).
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 27-30
    • Hayashi, S.1    Murakami, Y.2    Matsufuji, S.3
  • 14
    • 0028831608 scopus 로고
    • Antizyme autoregulatory frameshifting in decoding mammalian ornithine decarboxylase antizyme
    • Matsufuji, S. et al. Antizyme autoregulatory frameshifting in decoding mammalian ornithine decarboxylase antizyme. Cell 80, 51-60 (1995). Showed that translation of antizyme requires polyamine-stimulated frameshifting and defined the messenger RNA region that mediates that process.
    • (1995) Cell , vol.80 , pp. 51-60
    • Matsufuji, S.1
  • 15
    • 0033135202 scopus 로고    scopus 로고
    • Structure of mammalian ornithine decarboxylase at 1.6 a resolution: Stereochemical implications of PLP-dependent amino acid decarboxylases
    • Kern, A. D., Oliveira, M. A., Coffino, P. & Hackert, M. L. Structure of mammalian ornithine decarboxylase at 1.6 A resolution: stereochemical implications of PLP-dependent amino acid decarboxylases. Struct. Fold. Des. 7, 567-581 (1999).
    • (1999) Struct. Fold. Des. , vol.7 , pp. 567-581
    • Kern, A.D.1    Oliveira, M.A.2    Coffino, P.3    Hackert, M.L.4
  • 16
    • 0026714435 scopus 로고
    • Ornithine decarboxylase is degraded by the 26S proteasome without ubiquitination
    • Murakami, Y. et al. Ornithine decarboxylase is degraded by the 26S proteasome without ubiquitination. Nature 360, 597-599 (1992). Showed that purified 26S proteasomes degrade ODC, and that this process depends on antizyme but not ubiquitylation.
    • (1992) Nature , vol.360 , pp. 597-599
    • Murakami, Y.1
  • 17
    • 0032850746 scopus 로고    scopus 로고
    • ATP-dependent inactivation and sequestration of ornithine decarboxylase by the 26S proteasome are prerequisites for degradation
    • Murakami, Y., Matsufuji, S., Hayashi, S. I., Tanahashi, N. & Tanaka, K. ATP-dependent inactivation and sequestration of ornithine decarboxylase by the 26S proteasome are prerequisites for degradation. Mol. Cell. Biol. 19, 7216-7227 (1999).
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 7216-7227
    • Murakami, Y.1    Matsufuji, S.2    Hayashi, S.I.3    Tanahashi, N.4    Tanaka, K.5
  • 18
    • 0027512650 scopus 로고
    • Degradation of ornithine decarboxylase: Exposure of the C-terminal target by a polyamine-inducible inhibitory protein
    • Li, X. & Coffino, P. Degradation of ornithine decarboxylase: exposure of the C-terminal target by a polyamine-inducible inhibitory protein. Mol. Cell. Biol. 13, 2377-2383 (1993).
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 2377-2383
    • Li, X.1    Coffino, P.2
  • 19
    • 0024600672 scopus 로고
    • Prevention of rapid intracellular degradation of ODC by a carboxyl-terminal truncation
    • Ghoda, L., van Daalen Wetters, T., Macrae, M., Ascherman, D. & Coffino, P. Prevention of rapid intracellular degradation of ODC by a carboxyl-terminal truncation. Science 243, 1493-1495 (1989). Showed that a region of vertebrate ODC that is redundant for enzymatic activity is necessary for degradation.
    • (1989) Science , vol.243 , pp. 1493-1495
    • Ghoda, L.1    Van Daalen Wetters, T.2    Macrae, M.3    Ascherman, D.4    Coffino, P.5
  • 20
    • 0028144405 scopus 로고
    • Distinct domains of antizyme required for binding and proteolysis of ornithine decarboxylase
    • Li, X. & Coffino, P. Distinct domains of antizyme required for binding and proteolysis of ornithine decarboxylase. Mol. Cell. Biol. 14, 87-92 (1994). Identified distinct regions of antizyme that mediate target binding and degradation.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 87-92
    • Li, X.1    Coffino, P.2
  • 21
    • 0028884169 scopus 로고
    • Identification of an endogenous inhibitor of prostatic carcinoma cell growth
    • Smith, R. C., Litwin, M. S., Lu, Y. & Zetter, B. R. Identification of an endogenous inhibitor of prostatic carcinoma cell growth. Nature Med. 1, 1040-1045 (1995).
    • (1995) Nature Med. , vol.1 , pp. 1040-1045
    • Smith, R.C.1    Litwin, M.S.2    Lu, Y.3    Zetter, B.R.4
  • 22
    • 0033572568 scopus 로고    scopus 로고
    • Sensitivity to polyamine-induced growth arrest correlates with antizyme induction in prostate carcinoma cells
    • Koike, C., Chao, D. T. & Zetter, B. R. Sensitivity to polyamine-induced growth arrest correlates with antizyme induction in prostate carcinoma cells. Cancer Res. 59, 6109-6112 (1999). Indicated a possible function for antizyme in the regulation of prostate cell growth.
    • (1999) Cancer Res. , vol.59 , pp. 6109-6112
    • Koike, C.1    Chao, D.T.2    Zetter, B.R.3
  • 24
    • 0030755394 scopus 로고    scopus 로고
    • Activation of polyamine catabolism profoundly alters tissue polyamine pools and affects hair growth and female fertility in transgenic mice overexpressing spermidine/spermine N1-acetyltransferase
    • Pietila, M. et al. Activation of polyamine catabolism profoundly alters tissue polyamine pools and affects hair growth and female fertility in transgenic mice overexpressing spermidine/spermine N1-acetyltransferase. J. Biol. Chem. 272, 18746-18751 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 18746-18751
    • Pietila, M.1
  • 25
    • 0029050287 scopus 로고
    • Increased frequency of spontaneous skin tumors in transgenic mice which overexpresses ornithine decarboxylase
    • Megosh, L. et al. Increased frequency of spontaneous skin tumors in transgenic mice which overexpresses ornithine decarboxylase. Cancer Res. 55, 4205-4209 (1995).
    • (1995) Cancer Res. , vol.55 , pp. 4205-4209
    • Megosh, L.1
  • 26
    • 0346785230 scopus 로고    scopus 로고
    • Targeted antizyme expression protects transgenic mice from skin carcinogenesis
    • Feith, D. & Pegg, A. Targeted antizyme expression protects transgenic mice from skin carcinogenesis. Proc. Am. Assoc. Cancer Res. 41, 208 (2000).
    • (2000) Proc. Am. Assoc. Cancer Res. , vol.41 , pp. 208
    • Feith, D.1    Pegg, A.2
  • 27
    • 0034664956 scopus 로고    scopus 로고
    • Overexpression of antizyme in the hearts of transgenic mice prevents the isoprenaline-induced increase in cardiac ornithine decarboxylase activity, but does not prevent cardiac hypertrophy
    • MacKintosh, C., Feith, D., Shantz, L. & Pegg, A. Overexpression of antizyme in the hearts of transgenic mice prevents the isoprenaline-induced increase in cardiac ornithine decarboxylase activity, but does not prevent cardiac hypertrophy. Biochem. J. 350, 645-653 (2000).
    • (2000) Biochem. J. , vol.350 , pp. 645-653
    • MacKintosh, C.1    Feith, D.2    Shantz, L.3    Pegg, A.4
  • 28
    • 0034283845 scopus 로고    scopus 로고
    • Antizyme expression: A subversion of triplet decoding, which is remarkably conserved by evolution, is a sensor for an autoregulatory circuit
    • Ivanov, I., Gesteland, R. & Atkins, J. Antizyme expression: A subversion of triplet decoding, which is remarkably conserved by evolution, is a sensor for an autoregulatory circuit. Nucleic Acids Res. 28, 3185-3196 (2000).
    • (2000) Nucleic Acids Res. , vol.28 , pp. 3185-3196
    • Ivanov, I.1    Gesteland, R.2    Atkins, J.3
  • 29
    • 0033543664 scopus 로고    scopus 로고
    • Antizyme2 is a negative regulator of ornithine decarboxylase and polyamine transport
    • Zhu, C., Lang, D. W. & Coffino, P. Antizyme2 is a negative regulator of ornithine decarboxylase and polyamine transport. J. Biol. Chem. 274, 26425-26430 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 26425-26430
    • Zhu, C.1    Lang, D.W.2    Coffino, P.3
  • 30
    • 0034712739 scopus 로고    scopus 로고
    • Discovery of a spermatogenesis, stage specific, ornithine decarboxylase antizyme:antizyme 3
    • Ivanov, I., Rohrwasser, A., Terreros, D., Gesteland, R. & Atkins, J. Discovery of a spermatogenesis, stage specific, ornithine decarboxylase antizyme:antizyme 3. Proc. Natl Acad. Sci. USA 97, 4808-4813 (2000). Described a novel form of antizyme with a very restricted tissue distribution.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 4808-4813
    • Ivanov, I.1    Rohrwasser, A.2    Terreros, D.3    Gesteland, R.4    Atkins, J.5
  • 31
    • 0034098034 scopus 로고    scopus 로고
    • Identification and characterization of testis specific ornithine decarboxylase antizyme (OANTIZYME-t) gene: Expression in haploid germ cells and polyamine-induced frameshifting
    • Tosaka, Y. et al. Identification and characterization of testis specific ornithine decarboxylase antizyme (OANTIZYME-t) gene: Expression in haploid germ cells and polyamine-induced frameshifting. Genes to Cells 5, 265-276 (2000).
    • (2000) Genes to Cells , vol.5 , pp. 265-276
    • Tosaka, Y.1
  • 32
    • 0027504245 scopus 로고
    • Polyamines and regulation of spermatogenesis: Selective stimulation of late spermatogonia in transgenic mice overexpressing the human ornithine decarboxylase gene
    • Hakovirta, H. et al. Polyamines and regulation of spermatogenesis: selective stimulation of late spermatogonia in transgenic mice overexpressing the human ornithine decarboxylase gene. Mol. Endocrinol. 7, 1430-1436 (1993).
    • (1993) Mol. Endocrinol. , vol.7 , pp. 1430-1436
    • Hakovirta, H.1
  • 33
    • 0034640110 scopus 로고    scopus 로고
    • A proteasome howdunit: The case of the missing signal
    • Verma, R. & Deshaies, R. J. A proteasome howdunit: the case of the missing signal. Cell 101, 341-344 (2000).
    • (2000) Cell , vol.101 , pp. 341-344
    • Verma, R.1    Deshaies, R.J.2
  • 34
    • 0028296140 scopus 로고
    • Feedback repression of polyamine transport is mediated by antizyme in mammalian tissue-culture cells
    • Mitchell, J. L. A., Judd, G. G., Bareyal-Leyser, A. & Ling, S. Y. Feedback repression of polyamine transport is mediated by antizyme in mammalian tissue-culture cells. Biochem. J. 299, 19-22 (1994).
    • (1994) Biochem. J. , vol.299 , pp. 19-22
    • Mitchell, J.L.A.1    Judd, G.G.2    Bareyal-Leyser, A.3    Ling, S.Y.4
  • 35
    • 0027930451 scopus 로고
    • Antizyme delays the restoration by spermine of growth of polyamine-deficient cells through its negative regulation of polyamine transport
    • He, Y., Suzuki, T., Kashiwagi, K. & Igarashi, K. Antizyme delays the restoration by spermine of growth of polyamine-deficient cells through its negative regulation of polyamine transport. Biochem. Biophys. Res. Commun. 203, 608-614 (1994).
    • (1994) Biochem. Biophys. Res. Commun. , vol.203 , pp. 608-614
    • He, Y.1    Suzuki, T.2    Kashiwagi, K.3    Igarashi, K.4
  • 37
    • 0030020026 scopus 로고    scopus 로고
    • Cloning of antizyme inhibitor, a highly homologous protein to ornithine decarboxylase
    • Murakami, Y. Ichiba, T., Matsufuji, S. & Hayashi, S. Cloning of antizyme inhibitor, a highly homologous protein to ornithine decarboxylase. J. Biol. Chem. 271, 3340-3342 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 3340-3342
    • Murakami, Y.1    Ichiba, T.2    Matsufuji, S.3    Hayashi, S.4
  • 38
    • 0014323475 scopus 로고
    • Amine synthesis in rapidly growing tissues: Ornithine decarboxylase activity in regenerating rat liver, chick embryo, and various tumors
    • Russell, D. & Snyder, S. H. Amine synthesis in rapidly growing tissues: ornithine decarboxylase activity in regenerating rat liver, chick embryo, and various tumors. Proc. Natl Acad. Sci. USA 60, 1420-1427 (1968).
    • (1968) Proc. Natl Acad. Sci. USA , vol.60 , pp. 1420-1427
    • Russell, D.1    Snyder, S.H.2
  • 39
    • 0014512849 scopus 로고
    • Amine synthesis in regenerating rat liver: Extremely rapid turnover of ornithine decarboxylase
    • Russell, D. H. & Snyder, S. H. Amine synthesis in regenerating rat liver: extremely rapid turnover of ornithine decarboxylase. Mol. Pharmacol. 5, 253-262 (1969).
    • (1969) Mol. Pharmacol. , vol.5 , pp. 253-262
    • Russell, D.H.1    Snyder, S.H.2
  • 40
    • 0015612171 scopus 로고
    • Control of ornithine decarboxylase activity in stimulated human lymphocytes by putrescine and spermidine
    • Kay, J. E. & Lindsay, V. J. Control of ornithine decarboxylase activity in stimulated human lymphocytes by putrescine and spermidine. Biochem. J. 132, 791-796 (1973).
    • (1973) Biochem. J. , vol.132 , pp. 791-796
    • Kay, J.E.1    Lindsay, V.J.2
  • 41
    • 0020485107 scopus 로고
    • Purification and some properties of ornithine decarboxylase from rat liver
    • Kameji, T., Murakami, Y., Fujita, K. & Hayashi, S. Purification and some properties of ornithine decarboxylase from rat liver. Biochim. Biophys. Acta 717, 111-117 (1982).
    • (1982) Biochim. Biophys. Acta , vol.717 , pp. 111-117
    • Kameji, T.1    Murakami, Y.2    Fujita, K.3    Hayashi, S.4
  • 42
    • 0022425793 scopus 로고
    • Role of antizyme in degradation of ornithine decarboxylase in HTC cells
    • Murakami, Y. & Hayashi, S. Role of antizyme in degradation of ornithine decarboxylase in HTC cells. Biochem. J. 226, 893-896 (1985).
    • (1985) Biochem. J. , vol.226 , pp. 893-896
    • Murakami, Y.1    Hayashi, S.2
  • 43
    • 0025164449 scopus 로고
    • Antizyme analyses of ornithine decarboxylase antizyme mRNA with a cDNA cloned from rat liver
    • Matsufuji, S. et al. Antizyme analyses of ornithine decarboxylase antizyme mRNA with a cDNA cloned from rat liver. J. Biochem. 108, 365-371 (1990).
    • (1990) J. Biochem. , vol.108 , pp. 365-371
    • Matsufuji, S.1
  • 44
    • 0026577742 scopus 로고
    • Cloning and characterization of a rat gene encoding ornithine decarboxylase antizyme
    • Miyazak, Y., Matsufuji, S. & Hayashi, S. Cloning and characterization of a rat gene encoding ornithine decarboxylase antizyme. Gene 113, 191-197 (1992).
    • (1992) Gene , vol.113 , pp. 191-197
    • Miyazak, Y.1    Matsufuji, S.2    Hayashi, S.3
  • 45
    • 0026776758 scopus 로고
    • Destabilization of ornithine decarboxylase by transfected antizyme gene expression in hepatoma tissue culture cells
    • Murakami, Y. Matsufuji, S., Miyantizymeaki, Y. & Hayashi, S. Destabilization of ornithine decarboxylase by transfected antizyme gene expression in hepatoma tissue culture cells. J. Biol. Chem. 267, 13138-13141 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 13138-13141
    • Murakami, Y.1    Matsufuji, S.2    Miyantizymeaki, Y.3    Hayashi, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.